EC number:4.4.1.16

Enzyme

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     4. Lyases
        4.4 Carbon-sulfur lyases
            4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)
ID:4.4.1.16
Description:Selenocysteine lyase.
Alternative Name: Selenocysteine reductase.
Selenocysteine beta-lyase.
Cath: 1.10.260.50; 3.40.640.10; 3.90.1150.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.4.1.16
BRENDA Enzyme Link: BRENDA 4.4.1.16
KEGG Enzyme Link: KEGG4.4.1.16
BioCyc Enzyme Link: BioCyc 4.4.1.16
ExPASy Enzyme Link: ExPASy4.4.1.16
EC2PDB Enzyme Link: EC2PDB 4.4.1.16
ExplorEnz Enzyme Link: ExplorEnz 4.4.1.16
PRIAM enzyme-specific profiles Link: PRIAM 4.4.1.16
IntEnz Enzyme Link: IntEnz 4.4.1.16
MEDLINE Enzyme Link: MEDLINE 4.4.1.16

EC number:4.4.1.16

MSA:

4.4.1.16;
Phylogenetic Tree:

4.4.1.16;
Uniprot:
M-CSA:
RHEA:11632 AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine
RULE(radius=1) [*:1]-[CH2;+0:2]-[SeH;+0:3]>>[*:1]-[CH3;+0:2].[SeH-:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme.Mihara H, Kurihara T, Yoshimura T, Soda K, Esaki N1997 Sep 59278392
Selenocysteine lyase, a novel enzyme that specifically acts on selenocysteine. Mammalian distribution and purification and properties of pig liver enzyme.Esaki N, Nakamura T, Tanaka H, Soda K1982 Apr 256461656
Reaction mechanism and molecular basis for selenium/sulfur discrimination of selenocysteine lyase.Omi R, Kurokawa S, Mihara H, Hayashi H, Goto M, Miyahara I, Kurihara T, Hirotsu K, Esaki N2010 Apr 1620164179